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P62422 (PGK_WOLPM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase

EC=2.7.2.3
Gene names
Name:pgk
Ordered Locus Names:WD_1167
OrganismWolbachia pipientis wMel [Complete proteome] [HAMAP]
Taxonomic identifier163164 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeWolbachieaeWolbachia

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP-Rule MF_00145

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP-Rule MF_00145

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00145

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000146039

Regions

Nucleotide binding351 – 3544ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1171Substrate By similarity
Binding site1501Substrate By similarity
Binding site2001ATP By similarity
Binding site3211ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P62422 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3D2693F5491E0BF0

FASTA39843,305
        10         20         30         40         50         60 
MNIPSIENCD LHNKTVLLRV DFNVPIKDGE IRDVTRILRA LPTIQYLVNA SAKIIIISHF 

        70         80         90        100        110        120 
GRPKARDNNL SLKNVIDTLS QLLNKKVKFI DDCFGEKVQR AVSVMDAGDI ILLENLRFYK 

       130        140        150        160        170        180 
EEEQSDSNFA KQLASLADIY VNDAFSCSHR AHASISRITE FLPSYAGFCL QDELKYLEKA 

       190        200        210        220        230        240 
VSFKAKPITA IVGGAKISTK IKVLMKLTEK VNYLVLGGAI ANNFLSFSKV NIGKSFFQNG 

       250        260        270        280        290        300 
VDDLLHNILE TANKNNCKIV VPEDVLVAVN SDYSTSISRR TESILDGDII LDIGPQTLST 

       310        320        330        340        350        360 
ISSIIASSKT LLWNGPIGVF EHSAFASGTI GVMKIVSDLT HKGKLTSIIG GGDSLSAISA 

       370        380        390 
AGLADKDFTY VSTGGGAFLD WLSGDEMPGV AALQKRLD 

« Hide

References

[1]"Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements."
Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C., McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R., Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F., Nelson W.C. expand/collapse author list , Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R., Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H., O'Neill S.L., Eisen J.A.
PLoS Biol. 2:327-341(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017196 Genomic DNA. Translation: AAS14814.1.
RefSeqNP_966880.1. NC_002978.6.

3D structure databases

ProteinModelPortalP62422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING163164.WD1167.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS14814; AAS14814; WD_1167.
GeneID2738100.
KEGGwol:WD1167.
PATRIC24030931. VBIWolEnd21207_1155.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycWEND163164:GJ8W-1151-MONOMER.
UniPathwayUPA00109; UER00185.

Family and domain databases

Gene3D3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPMF_00145. Phosphoglyc_kinase.
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGK_WOLPM
AccessionPrimary (citable) accession number: P62422
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways